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  2. Hydrophobe - Wikipedia

    en.wikipedia.org/wiki/Hydrophobe

    The hydrophobic interaction is mostly an entropic effect originating from the disruption of the highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute, causing the water to compensate by forming a clathrate-like cage structure around the non-polar molecules. This structure is more highly ordered than free water ...

  3. Hydrophobic effect - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic_effect

    Dynamic hydrogen bonds between molecules of liquid water, the shape of the molecules is sometimes compared to that of boomerangs. The origin of the hydrophobic effect is not fully understood. Some argue that the hydrophobic interaction is mostly an entropic effect originating from the disruption of highly dynamic hydrogen bonds between ...

  4. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Protein–protein_interaction

    Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that ...

  5. Non-covalent interaction - Wikipedia

    en.wikipedia.org/wiki/Non-covalent_interaction

    [23] [24] [25] An essentially enthalpic hydrophobic effect materializes if a limited number of water molecules are restricted within a cavity; displacement of such water molecules by a ligand frees the water molecules which then in the bulk water enjoy a maximum of hydrogen bonds close to four.

  6. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Mostly they are connected to the active site by non-covalent bonds such as hydrogen bond or hydrophobic interaction. But sometimes a covalent bond can also form between them. For example, the heme in cytochrome C is bound to the protein through thioester bond. In some occasions, coenzymes can leave enzymes after the reaction is finished.

  7. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    The hydrophobic effect represents the tendency of water to exclude non-polar molecules. The effect originates from the disruption of highly dynamic hydrogen bonds between molecules of liquid water. Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect. However, a pure hydrocarbon molecule, for example hexane ...

  8. Disulfide - Wikipedia

    en.wikipedia.org/wiki/Disulfide

    It thus tends to form a covalent bond with another S − center to form S 2− 2 group, similar to elemental chlorine existing as the diatomic Cl 2. Oxygen may also behave similarly, e.g. in peroxides such as H 2 O 2. Examples: Hydrogen disulfide (S 2 H 2), the simplest inorganic disulfide; Disulfur dichloride (S 2 Cl 2), a distillable liquid.

  9. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    It is formed when atoms or molecules bind together by sharing of electrons. It often, but not always, involves some chemical bonding . In some cases, the associations can be quite strong—for example, the protein streptavidin and the vitamin biotin have a dissociation constant (reflecting the ratio between bound and free biotin) on the order ...